2PBJ
GSH-heme bound microsomal prostaglandin E synthase
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 475 |
Chain | Residue |
A | ARG137 |
A | ARG146 |
D | TYR287 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE HEM A 476 |
Chain | Residue |
A | SER247 |
A | ILE264 |
A | LEU293 |
A | GSH477 |
A | HOH497 |
A | HOH514 |
B | HOH502 |
A | THR109 |
A | PRO111 |
A | PHE112 |
A | PRO134 |
A | VAL243 |
A | HIS244 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GSH A 477 |
Chain | Residue |
A | TYR107 |
A | CYS110 |
A | PHE112 |
A | ARG146 |
A | LYS147 |
A | VAL148 |
A | PRO149 |
A | ASP164 |
A | SER165 |
A | HEM476 |
A | HOH481 |
A | HOH486 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 475 |
Chain | Residue |
B | ARG137 |
B | ARG146 |
C | TYR287 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM B 476 |
Chain | Residue |
B | THR109 |
B | PRO111 |
B | PHE112 |
B | PRO134 |
B | VAL243 |
B | HIS244 |
B | SER247 |
B | ILE264 |
B | LEU293 |
B | GSH477 |
B | HOH499 |
B | HOH510 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GSH B 477 |
Chain | Residue |
B | TYR107 |
B | CYS110 |
B | PHE112 |
B | ARG146 |
B | LYS147 |
B | VAL148 |
B | PRO149 |
B | ASP164 |
B | SER165 |
B | HEM476 |
B | HOH480 |
B | HOH485 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 475 |
Chain | Residue |
B | TYR287 |
C | ARG137 |
C | ARG146 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM C 476 |
Chain | Residue |
C | THR109 |
C | CYS110 |
C | PRO111 |
C | PHE112 |
C | PRO134 |
C | VAL243 |
C | HIS244 |
C | SER247 |
C | ILE264 |
C | LEU293 |
C | GSH477 |
C | HOH514 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GSH C 477 |
Chain | Residue |
C | TYR107 |
C | CYS110 |
C | PHE112 |
C | ARG146 |
C | LYS147 |
C | VAL148 |
C | ASP164 |
C | SER165 |
C | HEM476 |
C | HOH484 |
C | HOH502 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 475 |
Chain | Residue |
A | TYR287 |
D | ARG137 |
D | ARG146 |
site_id | BC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE HEM D 476 |
Chain | Residue |
D | THR109 |
D | CYS110 |
D | PRO111 |
D | PHE112 |
D | PRO134 |
D | VAL243 |
D | HIS244 |
D | SER247 |
D | ILE264 |
D | LEU293 |
D | GSH477 |
D | HOH492 |
site_id | BC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GSH D 477 |
Chain | Residue |
D | ARG146 |
D | LYS147 |
D | VAL148 |
D | ASP164 |
D | SER165 |
D | HEM476 |
D | TYR107 |
D | CYS110 |
D | PHE112 |
Functional Information from PROSITE/UniProt
site_id | PS00195 |
Number of Residues | 17 |
Details | GLUTAREDOXIN_1 Glutaredoxin active site. LYqyktCPFCskVrafL |
Chain | Residue | Details |
A | LEU104-LEU120 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17585783 |
Chain | Residue | Details |
A | VAL148 | |
C | VAL148 | |
C | ASP164 | |
D | VAL148 | |
D | ASP164 | |
A | ASP164 | |
B | VAL148 | |
B | ASP164 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9H7Z7 |
Chain | Residue | Details |
A | SER95 | |
B | SER95 | |
C | SER95 | |
D | SER95 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 192 |
Chain | Residue | Details |
A | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
A | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | PHE112 | electrostatic stabiliser, hydrogen bond donor |
A | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 192 |
Chain | Residue | Details |
B | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
B | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
B | PHE112 | electrostatic stabiliser, hydrogen bond donor |
B | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 192 |
Chain | Residue | Details |
C | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
C | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
C | PHE112 | electrostatic stabiliser, hydrogen bond donor |
C | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 192 |
Chain | Residue | Details |
D | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
D | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
D | PHE112 | electrostatic stabiliser, hydrogen bond donor |
D | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |